ID C0ZCE8_BREBN Unreviewed; 367 AA.
AC C0ZCE8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN Name=tyrA {ECO:0000313|EMBL:BAH43457.1};
GN OrderedLocusNames=BBR47_24800 {ECO:0000313|EMBL:BAH43457.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH43457.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH43457.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001162};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005067}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007964}.
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DR EMBL; AP008955; BAH43457.1; -; Genomic_DNA.
DR RefSeq; WP_012686164.1; NC_012491.1.
DR AlphaFoldDB; C0ZCE8; -.
DR STRING; 358681.BBR47_24800; -.
DR KEGG; bbe:BBR47_24800; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_1_9; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000001877; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04909; ACT_PDH-BS; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR003099; Prephen_DH.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAH43457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001877};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 4..292
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 297..367
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 367 AA; 40377 MW; 9B602DCBE21B48A8 CRC64;
MKKTTITVIG VGLIGGSIAL SMRRDPNIRV VGYDLRQDCL DKALTLGVIH AGTTDLQTAV
REANVIFLAS PVEQIVPTIR SLVEMELQPG VIITDVGSTK AGIVTQAADV IPDHVTFIGG
HPMAGSHKSG VEAASDRLME NAYYVLTPAP GTSVEKVKQL SELLTLTRAK VVQMDAASHD
QVVGAVSHFP HILASALVNL VAGYDEENAW HTTLAAGGFR DITRIASSNP QMWRDILLQN
RDPILKIAKD WANALEDVVH LVEQGDPEGI EHFFKTAREF RDSLPERKTG ALPPLNDLYI
DIPDHPGEIG RITTLLGARN INITNLQIRE TREDIFGVLR ITFHSQQELE KGEEVLRFFD
YNVYKRT
//
